This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Trommer's longtime cooperation partner, Professor Raghavan Varadaran from the Indian Institute of Science in Bangalore, India, has recently shown that maltose binding protein (MBP) from E. coli does bind maltose even in its molten globule state, although with substantially reduced affinity. The native protein of which the X-ray structure is known, is devoid of cysteines. We have seven different mutants with two cysteines each, which can be spin-labeled and some of them have already been modified with the MTS label. Distances as derived from the X-ray structure vary from 14 to 31 [unreadable]. Hence, we want to compare distances in the native protein with those in the molten globule state. To this end we will carry out low temperature cw EPR as well as DEER measurements at X-band first in Kaiserslautern. For other frequencies as well as DQC we will perform measurement at ACERT.